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At least 91 records · Page 5Linked to original sources
PubMed1992

Appearance of Ulex europaeus agglutinin-1 and Griffonia simplicifolia agglutinin-1 binding sites on cancer cells in sigmo-rectal polyps.

Ninety-three polypectomized cases from the sigmo-rectal region were examined by lectin histochemistry. On the apical surface, the UEA-1 binding sites were positive in 24/29 carcinomas and in 25/62 adenomas; while the GSA-1 binding sites were positive in 16/29 carcinomas and in 0/62 adenomas. In 2 non-neoplastic polyps, only one case was UEA-1 positive; none was GSA-1 positive. In neighbouring regions, adenomas adjacent to carcinomas were UEA-1 positive in 9/27 cases and GSA-1 positive in 3/37 cases. Thus, the GSA-1 binding sites were expressed more specifically on carcinomas. In the Golgi area, none of the polyps was UEA-1 positive while most of the cells showing GSA-1 positivity were apt to do so within the cells without showing GSA-1 positivity on the apical surface. There were no correlations between the positive rate of the lectin binding sites on the apical surface and the stage of cancer development or the histology of the adenoma on which a cancer developed. The meaning of this restricted appearance of the GSA-1 binding sites on the cancer cell surface was discussed in relation to observations previously reported in the literature.

Adenocarcinoma↗
PubMed1987

Hemagglutinins and bacterial agglutinins of earthworms.

The biological roles of invertebrate agglutinins have been and remain an unresolved subject of controversy. Classical studies on agglutinins, beginning with the pioneer work of Noguchi (1903) on Limulus polyphemus and Homarus americanus have emphasized their hemagglutinating properties, an approach that has been criticized for its lack of biological relevance. While erythrocyte agglutination has proven useful for determining various properties of invertebrate agglutinins, it does not address the question of their natural function. More recently, invertebrate agglutinins have been investigated for their ability to interact with pathogenic agents such as bacteria (for review, see Pistole, 1982), yeast (Van der Knapp et al., 1982; Renwrantz and Stahmer, 1983) and parasitic protozoans (Ingram et al., 1984). In addition, the possible relationship of agglutinins to defense mechanisms of both vertebrates and invertebrates has been indicated by the observation that limulin, the major agglutinin of Limulus polyphemus, bears a number of similarities to vertebrate C-reactive proteins (Robey and Liu, 1981). In annelids, there have been no studies on bacterial agglutinins prior to our work with Lumbricus (Stein et al., 1985; Stein et al., submitted). Earthworms are particularly appropriate for studying bacterial agglutinins since their coelomic fluid contains constant low levels of bacteria and fungal spores, and their agglutinins are both naturally occurring and inducible. Although our initial studies on Lumbricus agglutinins were directed toward their hemagglutinating properties, our recent observations using bacteria have allowed us to reach the following conclusions: 1) Lumbricus coelomic fluid normally contains agglutinins against both erythrocytes and bacteria. After injecting worms with either erythrocytes or bacteria, agglutinin titers increase in coelomic fluid. This increase appears to be due to both an increase in numbers of agglutinins as well as levels of specific agglutinins. 2) Absorption studies, temperature effects and sugar inhibition analyses suggest that agglutinins which bind to erythrocytes are identical to bacterial agglutinins, but there are additional agglutinins capable of reacting only with bacteria. 3) The inducibility and bacterial binding properties of Lumbricus agglutinins suggest that they serve an immune function by participating in the earthworm's defense against bacterial infection. In this sense, the agglutinins serve as a humoral surveillance system that entraps and prevents the multiplication of pathogenic bacteria.

Agglutinins↗
PubMed1982

B-cell neoplasms with homogeneous cold-reacting antibodies (cold agglutinins).

Among 78 patients with persistent cold agglutinins, 31 had lymphoma, 13 had macroglobulinemia of Waldenstrom, six had chronic lymphocytic leukemia and 28 had chronic cold agglutinin disease. The average age was over 60 years. Patients wit chronic cold agglutinin disease had more hemolytic crises, bleeding and Raynaud's phenomena, and less frequently lymphadenopathy or hepatosplenomegaly. The frequency of anemia, positive Coombs test results, cryoglobulinemia and Bence Jones proteinuria was similar in the various groups. Survival time from diagnosis was on average two years in lymphoma, two and a half years in Waldenstrom's macroglobulinemia, more than six years in chronic lymphocytic leukemia and more than five years in chronic cold agglutinin disease. Anti-I were common in chronic cold agglutinin disease (74 percent) and rare in other groups (32 to 33 percent). Anti-I and other cold agglutinins were rare in chronic cold agglutinin disease and common in lymphoma and Waldenstrom's macroglobulinemia. In chronic cold agglutinin disease, and in Waldenstrom's macroglobulinemia, cold agglutinins usually had K light chains--92 percent and 71 percent, respectively--whereas in lymphoma, 71 percent of cold agglutinins had lambda light chains. The type of light chains related to the specifically of cold agglutinins: 58 percent of IgM/K were anti-I, 75 percent of IgM/lambda had other specificities. Cold agglutinins were cytotoxic to autologous and allogeneic cells were killed implying that the former may be precoated in vivo with the antibodies. In conclusion, conditions with persistent cold agglutinins are a spectrum that varies from "benign" autoimmune-like chronic cold agglutinin disease to malignant lymphoma. Marked differences in the light chain type of cold agglutinins, specificity toward membranous antigens and severity of clinical manifestations were noted in benign and malignant varieties.

Adult↗
PubMed2000

Systemic effect of peanut agglutinin following intravenous infusion into rats.

BACKGROUND: Ingested peanut agglutinin stimulates colonic proliferation in humans. In rats, ingested peanut agglutinin stimulates hormone release and proliferation in the small and large intestines. Peanut agglutinin is absorbed into the circulation but little is known about the systemic effect of this lectin. Therefore, we studied the effect of intravenous peanut agglutinin on hormone release and intestinal growth. METHOD: Six rats per group received peanut agglutinin infusion at 0, 2, 20 or 200 microg/rat/day for 6 days via the right jugular vein. Organ weights were measured, pancreatic enzymes, DNA, RNA and protein levels were analysed. Plasma hormones were measured by radioimmunoassay. All tissues were examined histologically. Small intestinal and colonic proliferation rates were estimated by metaphase arrest. RESULTS: High-dose peanut agglutinin significantly reduced the wet weight of the stomach by 7% (P < 0.05) and large intestine by 10% (P < 0.05). Peanut agglutinin dose-dependently released enteroglucagon; low-, medium- and high-dose by 64%, 126% (P < 0.01) and 180% (P < 0.01), respectively, and glucagon-like peptide-1 by 127% (P < 0.01), 169% (P < 0.01) and 315% (P < 0.001), respectively. Peanut agglutinin had no effect on cholesystokinin, gastrin or insulin levels. Peanut agglutinin, low-, medium- and high-dose stimulated proliferation in the mid colon by 42% (P < 0.01), 30% and 38%, respectively. Only high-dose peanut agglutinin stimulated proliferation in the distal colon by 54% (P < 0.01). No histological changes were evident in any tissue. CONCLUSION: Intravenous peanut agglutinin released hormones and stimulated colonic proliferation. Proliferation of the small intestine seen after ingestion of peanut agglutinin in previous studies appears to require luminal contact between enterocytes and the lectin. Possible clinical applications include reversal of atrophy during total parenteral nutrition, anastomotic healing after surgery and restoration of mucosa integrity in colitis.

Animals↗